α-Crystallin and ATP facilitate the in vitro renaturation of xylanase: Enhancement of refolding by metal ions

Protein Science

Volumn 11, Issue 11, 2002, Pages 2727-2734

  Nath, Devyani ^a   Rawat, Urmila ^a   Anish, Ramakrishnan ^a   Rao, Mala ^a  

^a NATIONAL CHEMICAL LABORATORY   (India)

Author keywords

crystallin; ATP; Ca2+; Refolding; Xylanase

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ADENOSINE TRIPHOSPHATE; ADENYLYLIMIDODIPHOSPHATE; ALPHA CRYSTALLIN; CALCIUM; CHAPERONE; HEAT SHOCK PROTEIN; METAL ION; XYLAN ENDO 1,3 BETA XYLOSIDASE; BACTERIAL PROTEIN; ION; METAL; XYLAN 1,4 BETA XYLOSIDASE;

ARTICLE; BACILLUS; COMPLEX FORMATION; DISSOCIATION; ENZYME RENATURATION; FLUORESCENCE; HYDROLYSIS; HYDROPHOBICITY; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; CHEMISTRY; ENZYME ACTIVATION; ENZYMOLOGY; METABOLISM; PROTEIN DENATURATION; PROTEIN RENATURATION; SPECTROFLUOROMETRY; TEMPERATURE;

ADENOSINE TRIPHOSPHATE; ALPHA-CRYSTALLINS; BACILLUS; BACTERIAL PROTEINS; ENZYME ACTIVATION; IONS; METALS; MOLECULAR CHAPERONES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; XYLAN ENDO-1,3-BETA-XYLOSIDASE; XYLOSIDASES;

EID: 0036838853     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0213802     Document Type: Article

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